Phosphorylation of myosin II regulatory light chain controls its accumulation, not that of actin, at the contractile ring in HeLa cells

Kondo, Tomo; Itakura, Shiho; Hamao, Kozue; Hosoya, Hiroshi

doi:10.1016/j.yexcr.2012.02.009

Cited by 8 publications

(10 citation statements)

References 55 publications

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“…Therefore, using inhibitors of actin dynamics, we tested whether actin was required for the recruitment or docking of mitochondria to the cleavage furrow (Figure 5 and Movie S3). Cells were treated with either DMSO as a control or Latrunculin or Jasplakinolide to depolymerize or stabilize actin respectively (Figure S2, top row, and Figure S3) [28]–[30]. As expected, mitochondria were recruited to the cleavage furrow and away from the cell poles in DMSO-treated control cells (Figure 5A, top row, and Figure 5B, left panel).…”

Section: Resultsmentioning

confidence: 54%

Mitochondria Localize to the Cleavage Furrow in Mammalian Cytokinesis

Lawrence

Mandato

2013

PLoS ONE

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Mitochondria are dynamic organelles with multiple cellular functions, including ATP production, calcium buffering, and lipid biosynthesis. Several studies have shown that mitochondrial positioning is regulated by the cytoskeleton during cell division in several eukaryotic systems. However, the distribution of mitochondria during mammalian cytokinesis and whether the distribution is regulated by the cytoskeleton has not been examined. Using live spinning disk confocal microscopy and quantitative analysis of mitochondrial fluorescence intensity, we demonstrate that mitochondria are recruited to the cleavage furrow during cytokinesis in HeLa cells. After anaphase onset, the mitochondria are recruited towards the site of cleavage furrow formation, where they remain enriched as the furrow ingresses and until cytokinesis completion. Furthermore, we show that recruitment of mitochondria to the furrow occurs in multiple mammalian cells lines as well as in monopolar, bipolar, and multipolar divisions, suggesting that the mechanism of recruitment is conserved and robust. Using inhibitors of cytoskeleton dynamics, we show that the microtubule cytoskeleton, but not actin, is required to transport mitochondria to the cleavage furrow. Thus, mitochondria are specifically recruited to the cleavage furrow in a microtubule-dependent manner during mammalian cytokinesis. Two possible reasons for this could be to localize mitochondrial function to the furrow to facilitate cytokinesis and / or ensure accurate mitochondrial inheritance.

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Section: Resultsmentioning

confidence: 54%

Mitochondria Localize to the Cleavage Furrow in Mammalian Cytokinesis

Lawrence

Mandato

2013

PLoS ONE

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“…For time-lapse imaging, HeLa cells were cultured in a glass-based dish (Asahi Glass, Tokyo, Japan). After 1 day, cells were observed by using FV1000-D microscope as previously described [66]. Differential interference contrast microscopic images were acquired every minute for 3 h. All acquired images were processed with Adobe Photoshop.…”

Section: Methodsmentioning

confidence: 99%

Aurora B but Not Rho/MLCK Signaling Is Required for Localization of Diphosphorylated Myosin II Regulatory Light Chain to the Midzone in Cytokinesis

et al. 2013

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Non-muscle myosin II is stimulated by monophosphorylation of its regulatory light chain (MRLC) at Ser19 (1P-MRLC). MRLC diphosphorylation at Thr18/Ser19 (2P-MRLC) further enhances the ATPase activity of myosin II. Phosphorylated MRLCs localize to the contractile ring and regulate cytokinesis as subunits of activated myosin II. Recently, we reported that 2P-MRLC, but not 1P-MRLC, localizes to the midzone independently of myosin II heavy chain during cytokinesis in cultured mammalian cells. However, the mechanism underlying the distinct localization of 1P- and 2P-MRLC during cytokinesis is unknown. Here, we showed that depletion of the Rho signaling proteins MKLP1, MgcRacGAP, or ECT2 inhibited the localization of 1P-MRLC to the contractile ring but not the localization of 2P-MRLC to the midzone. In contrast, depleting or inhibiting a midzone-localizing kinase, Aurora B, perturbed the localization of 2P-MRLC to the midzone but not the localization of 1P-MRLC to the contractile ring. We did not observe any change in the localization of phosphorylated MRLC in myosin light-chain kinase (MLCK)-inhibited cells. Furrow regression was observed in Aurora B- and 2P-MRLC-inhibited cells but not in 1P-MRLC-perturbed dividing cells. Furthermore, Aurora B bound to 2P-MRLC in vitro and in vivo. These results suggest that Aurora B, but not Rho/MLCK signaling, is essential for the localization of 2P-MRLC to the midzone in dividing HeLa cells.

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“…MRLC phosphorylation affects protein-protein interactions and muscle relaxation through changing the function and structure of the actomyosin (Obermann et al, 1997;Zhi et al, 2005;Ryder et al, 2007). It has also been reported that phosphorylation tentatively controls MRLC aggregation in mammalian cells (Kondo et al, 2012). For instance, phosphorylation of myosin changes the conformation of the myosin head, which in turn regulates actomyosin dissociation and ATPase activity (Pemrick, 1980;Vibert & Cohen, 1988).…”

Section: Phosphorylation Of Mrlc Regulates Actomyosin Dissociationmentioning

confidence: 99%

“…It was also reported that diphosphorylation MRLC generated stronger forces in actomyosin than non-phosphorylated MRLC, indicating that phosphorylation of MRLC inhibited actomyosin dissociation (Mizutani et al, 2006;Kampourakis et al, 2016). In addition, phosphorylation of MRLC regulates myosin aggregation in mammalian cells (Kondo et al, 2012). For instance, phosphorylation of myosin alters the conformation of myosin head, which in turn might regulate actomyosin dissociation and ATPase activity (Pemrick, 1980;Vibert & Cohen, 1988).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of myosin regulatory light chain affects actomyosin dissociation and myosin degradation

Cao

Hou

Shen

et al. 2019

Int J of Food Sci Tech

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Summary This research aimed to investigate the influence of myosin regulatory light chain (MRLC) phosphorylation on actomyosin dissociation and myosin degradation in post‐mortem ovine longissimus thoracis (LT) muscle with a purpose for strategies to improve meat quality in practice. Data obtained show that the highest actomyosin dissociation occurred at 48 h post‐mortem. Based on the cluster analysis of the actomyosin dissociation degree at 48 h post‐mortem, samples were divided into high, middle and low‐actomyosin dissociation groups. During 0.5–72 h post‐mortem, the phosphorylation level of MRLC significantly decreased (P < 0.05), while actomyosin dissociation, and degradation of MRLC and myosin heavy chains (MHC) significantly increased (P < 0.05). The level of MRLC phosphorylation was negatively correlated with the degree of actomyosin dissociation (r = −0.794, P < 0.05), and the degradation of MRLC (r = −0.764, P < 0.05) and MHC (r = −0.826, P < 0.05). In conclusion, phosphorylation of MRLC may regulate actomyosin dissociation, as well as degradation of MRLC and MHC.

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Phosphorylation of myosin II regulatory light chain controls its accumulation, not that of actin, at the contractile ring in HeLa cells

Cited by 8 publications

References 55 publications

Mitochondria Localize to the Cleavage Furrow in Mammalian Cytokinesis

Mitochondria Localize to the Cleavage Furrow in Mammalian Cytokinesis

Aurora B but Not Rho/MLCK Signaling Is Required for Localization of Diphosphorylated Myosin II Regulatory Light Chain to the Midzone in Cytokinesis

Phosphorylation of myosin regulatory light chain affects actomyosin dissociation and myosin degradation

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